Abstract
Abstract Serum and urinary albumin from patients with renal disease have been fractionated by isoelectric focusing in granulated gels in 4 fractions named A1, A2, A3 and A4. When analyzed by isoelectric focusing in conventional ultrathin gels containing 2 M urea, only A4 showed a band with pI = 6.1, which is the isoionic point of albumin. It was concluded that A4 is responsible for the microheterogeneity of albumin in gels containing low concentrations of urea. Preparative isoelectric focusing in granulated gels can be employed for molecular studies on albumin in renal diseases.
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